Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy - Test2 - elhamkhani - TriplyDB

Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy

Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy

http://www.wikidata.org/entity/Q27739077

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Balancing solvation and intramolecular interactions: toward a consistent generalized Born force field Insights into domain-domain motions in proteins and RNA from solution NMR The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA.Structural Assembly of Multidomain Proteins and Protein Complexes Guided by the Overall Rotational Diffusion Tensor Liquid-crystal NMR structure of HIV TAR RNA bound to its SELEX RNA aptamer reveals the origins of the high stability of the complex Improving NMR protein structure quality by Rosetta refinement: A molecular replacement study Two Structurally Independent Domains of E. coli NusG Create Regulatory Plasticity via Distinct Interactions with RNA Polymerase and Regulators High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins Automated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithm Correlated inter-domain motions in adenylate kinase Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution Using the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes.Impact of 15N R2/R1 relaxation restraints on molecular size, shape, and bond vector orientation for NMR protein structure determination with sparse distance restraints The use of residual dipolar coupling in studying proteins by NMR.Parameterization of solvent-protein interaction and its use on NMR protein structure determination Design of single-layer beta-sheets without a hydrophobic core.Structural insights from (15)N relaxation data for an anisotropic collagen peptide.Determining interdomain structure and dynamics of a retroviral capsid protein in the presence of oligomerization: implication for structural transition in capsid assembly.Direct use of 15N relaxation rates as experimental restraints on molecular shape and orientation for docking of protein-protein complexes.Water proton spin saturation affects measured protein backbone 15N spin relaxation rates.New methods of structure refinement for macromolecular structure determination by NMR.Deriving quantitative dynamics information for proteins and RNAs using ROTDIF with a graphical user interface.Exposing the Moving Parts of Proteins with NMR Spectroscopy.Advances in the determination of nucleic acid conformational ensembles Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution.NMR studies of nucleic acid dynamics An overview of tools for the validation of protein NMR structures.Equivalence between Euler angle conventions for the description of tensorial interactions in liquid NMR: application to different software programs.The amino-terminal domain of human STAT4. Overproduction, purification, and biophysical characterization.Xplor-NIH for Molecular Structure Determination from NMR and Other Data Sources.Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO.A solution SAXS study of Borrelia burgdorferi OspA, a protein containing a single-layer beta-sheet.Fast approximations of the rotational diffusion tensor and their application to structural assembly of molecular complexes.The structure of the flock house virus B2 protein, a viral suppressor of RNA interference, shows a novel mode of double-stranded RNA recognition.Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.Structure and dynamics of the tetrameric mnt repressor and a model for its DNA complex.The domain architecture of the PtkA, the first tyrosine kinase from Mycobacterium tuberculosis differs from the conventional kinase architecture.Modern High Resolution NMR for the Study of Structure, Dynamics and Interactions of Biological Macromolecules Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions Nuclear Magnetic Resonance Methods for Studying Soluble, Fibrous, and Membrane-Embedded Proteins

P2860

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P2860

Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy

http://www.wikidata.org/entity/Q27739077

description

1997 nî lūn-bûn

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1997 թուականի Յունիսին հրատարակուած գիտական յօդուած

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1997年の論文

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Defining long range order in N ...... otational diffusion anisotropy

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Defining long range order in N ...... otational diffusion anisotropy

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Defining long range order in N ...... otational diffusion anisotropy

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Defining long range order in N ...... otational diffusion anisotropy

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Defining long range order in N ...... otational diffusion anisotropy

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Defining long range order in N ...... otational diffusion anisotropy

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Defining long range order in N ...... otational diffusion anisotropy

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Defining long range order in N ...... otational diffusion anisotropy

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Nature structural biology

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Defining long range order in N ...... otational diffusion anisotropy

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A Bax

http://www.w3.org/2001/XMLSchema#string

A M Gronenborn

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D S Garrett

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G M Clore

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N Tjandra

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P2860

PROCHECK: a program to check the stereochemical quality of protein structures

Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR

MOLMOL: a program for display and analysis of macromolecular structures

The impact of direct refinement against 13C alpha and 13C beta chemical shifts on protein structure determination by NMR.

The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.

Deviations from planarity of the peptide bond in peptides and proteins.

Magnetic Field Dependence of Nitrogen−ProtonJSplittings in15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar Coupling

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443-9

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10.1038/NSB0697-443

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6

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4

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14030565

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